1. AP Biology Exam Review: Learning Objective Focus – Due Wednesday, April 29 th – 4 th Quarter Test Grade 1) Choose an AP Biology Learning Objective (LO) from your table. 2) Using your notes, the Internet, and PowerPoint, create ONE PowerPoint slide that reviews your chosen Learning Objective. This slide MUST include: A) A statement of the Learning Objective B) A statement of the connected Science Practice (SP) C) A statement that explains the Learning Objective in terms of curriculum content and makes a connection between the LO and the related SP. D) An original multiple-choice question that tests students’ knowledge of the LO. E) An original FRQ-style essay question that tests students’ knowledge of the LO. F) At least one labeled diagram or figure that further explains or provides a visualization of curriculum content directly related to the LO. G) A second “ANSWER KEY” slide tha contains the correct answer for the multiple choice question and an appropriate and complete for the FRQ. ***See example slide for reference.*** 4) Use the following link to find more information on your LO and SP: media.collegeboard.com/digitalServices/pdf/ap/10b_2727_AP_Biology_CF_WEB_110128.pdf 5) Email your PowerPoint slide to me (sbennett2@wsfcs.k12.nc.us) as a file attachment. Includesbennett2@wsfcs.k12.nc.us your full name, period & learning objective number in the subject line. I’ll compile a class set of these slides and post them on my website.

2. LO 4.1: The student is able to explain the connection between the sequence and the subcomponents of a biological polymer and its properties. SP 7.1: The student can connect phenomena and models across spatial and temporal scales. Explanation: In proteins, for example, the specific order of amino acids in a polypeptide interacts with the environment to determine the overall shape of the protein, which also involves the secondary, tertiary, and quaternary structure and, thus, its function. The R group of each amino acid in the polypeptide can be categorized by its chemical properties (hydrophilic, hydrophobic, ionic, etc.) and the interactions of these R groups determine structure and function of that region of the protein. Enzymes are examples of proteins whose functions rely on their structure. This relationship between the sequence of the subcomponents and the properties of the molecule is also evident in nucleic acids, lipids, and carbohydrates. M.C. Question: Which of the following statements concerning unsaturated fats is true? A) They are more common in animals than in plants. B) They have only single bonds in the carbon chains of their fatty acid tails. C) They’re generally a solid at room temperature b/c their molecules are closely packed together. D) They’re generally a liquid at room temperature b/c their molecules have kinks caused by double bonds. Learning Log/FRQ-style Question: Suppose you have placed a protein in an aqueous environment. Where would you expect to find a region that is rich in polar amino acids? Why? A region rich in non-polar amino acids? Why? Draw and label this hypothetical protein.

3. ANSWER KEY– LO 4.1 Which of the following statements concerning unsaturated fats is true? A) They are more common in animals than in plants. B) They have only single bonds in the carbon chains of their fatty acid tails. C) They’re generally a solid at room temperature b/c their molecules are closely packed together. D) They’re generally a liquid at room temperature b/c their molecules have kinks caused by double bonds. (sample drawing) Suppose you have placed a protein in an aqueous environment. Where would you expect to find a region that is rich in polar amino acids? Why? A region rich in non-polar amino acids? Why? Draw and label this hypothetical protein. A protein in an aqueous environment should be expected to have regions containing polar amino acids near the surface of the macromolecule because these polar amino acids will interact with the polar water molecules found within the aqueous solution. The regions containing non-polar amino acids should be found within the interior of the macromolecule because these non-polar amino acids will want to interact with each other, as far away from the presence of the polar aqueous environment as is possible.